Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration

The secondary structure of a 55-residue fragment of the mouse prion protein, MoPrP(89–143), was studied in randomly aggregated (dried from water) and fibrillar (precipitated from water/acetonitrile) forms by (13)C solid-state NMR. Recent studies have shown that the fibrillar form of the P101L mutant...

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Hlavní autoři: Laws, David D., Bitter, Hans-Marcus L., Liu, Kai, Ball, Haydn L., Kaneko, Kiyatoshi, Wille, Holger, Cohen, Fred E., Prusiner, Stanley B., Pines, Alexander, Wemmer, David E.
Médium: Artigo
Jazyk:Inglês
Vydáno: The National Academy of Sciences 2001
Témata:
Biological Sciences
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC58790/
https://ncbi.nlm.nih.gov/pubmed/11562491
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.201404298
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